| Value |
4
years
|
| Organism |
Generic |
| Reference |
Wolfenden R, Snider MJ. The depth of chemical time and the power of enzymes as catalysts. Acc Chem Res. 2001 Dec34(12):938-45. p.940 table 1 Table - link PubMed ID11747411
|
| Primary Source |
Radzicka, A. Wolfenden, R. Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases. J. Am. Chem. Soc. 1996, 118, 6105-6109. |
| Method |
Carboxypeptidase, endopeptidase and dipeptide cleavage reactions were modeled by a suitable derivative of glycylglycine, and could be followed by proton NMR in the temperature range near 150 °C. In each case, the linear Arrhenius plot yielded a half-time of approximately 400 years at 25 °C (primary source). |
| Comments |
Value calculated by dividing halftime of spontaneous protein hydrolysis at 25°C, 400 years (BNID 105352) by number of amino acids in RNase A. Halftime of hydrolysis event of peptide bond in RNase A at 100°C is 7 hours. See table link |
| Entered by |
Uri M |
| ID |
105356 |